Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Alexander F. Schubert"'
Autor:
Eric M. Kofoed, Russell E. Vance, Man-Wah Tan, Tommy K. Cheung, Yuxin Liang, Giovanni Luchetti, Christopher M. Rose, Justin L. Roncaioli, Elizabeth Skippington, Kim Newton, Janina Reeder, Vishva M. Dixit, Alexander F. Schubert, Rohit Reja, Benjamin Haley, Nobuhiko Kayagaki, Roberto A. Chavez, Isabelle Lehoux, Joshua D. Webster
Publikováno v:
Cell Host Microbe
Summary The pore-forming protein gasdermin D (GSDMD) executes lytic cell death called pyroptosis to eliminate the replicative niche of intracellular pathogens. Evolution favors pathogens that circumvent this host defense mechanism. Here, we show that
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::35137471dfdcf537a68417e65484c59f
https://europepmc.org/articles/PMC9122893/
https://europepmc.org/articles/PMC9122893/
Autor:
Zhong Yan Gan, Sylvie Callegari, Simon A. Cobbold, Thomas R. Cotton, Michael J. Mlodzianoski, Alexander F. Schubert, Niall D. Geoghegan, Kelly L. Rogers, Andrew Leis, Grant Dewson, Alisa Glukhova, David Komander
Publikováno v:
Nature. 602(7896)
Mutations in the protein kinase PINK1 lead to defects in mitophagy and cause autosomal recessive early onset Parkinson's disease
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6588c3951991931576f31094feab91db
https://pubmed.ncbi.nlm.nih.gov/35293391
https://pubmed.ncbi.nlm.nih.gov/35293391
Autor:
Zhong Yan Gan, Sylvie Callegari, Simon A. Cobbold, Thomas R. Cotton, Michael J. Mlodzianoski, Alexander F. Schubert, Niall D. Geoghegan, Kelly L. Rogers, Andrew Leis, Grant Dewson, Alisa Glukhova, David Komander
Publikováno v:
Nature. 603:E33-E33
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b24df92c26e971998cad502fd60dbf68
https://doi.org/10.1038/s41586-022-04591-7
https://doi.org/10.1038/s41586-022-04591-7
Autor:
Justine V. Nguyen, David Komander, Kay Hofmann, Cameron G. Roberts, Daniel J. Sanderson, Jonathan N. Pruneda, Alexander F. Schubert, Paul P. Geurink, Huib Ovaa, Tyler G. Franklin, Lauren N. Miller
Publikováno v:
EMBO Journal, 39(15). WILEY
EMBO Journal. WILEY
EMBO Journal
The EMBO Journal
EMBO Journal. WILEY
EMBO Journal
The EMBO Journal
Manipulation of host ubiquitin signaling is becoming an increasingly apparent evolutionary strategy among bacterial and viral pathogens. By removing host ubiquitin signals, for example, invading pathogens can inactivate immune response pathways and e
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8b8982748e31a20708b4ee506b072a18
http://hdl.handle.net/1887/3182563
http://hdl.handle.net/1887/3182563
Autor:
Alexander D, Gitlin, Klaus, Heger, Alexander F, Schubert, Rohit, Reja, Donghong, Yan, Victoria C, Pham, Eric, Suto, Juan, Zhang, Youngsu C, Kwon, Emily C, Freund, Jing, Kang, Anna, Pham, Roger, Caothien, Natasha, Bacarro, Trent, Hinkle, Min, Xu, Brent S, McKenzie, Benjamin, Haley, Wyne P, Lee, Jennie R, Lill, Merone, Roose-Girma, Monika, Dohse, Joshua D, Webster, Kim, Newton, Vishva M, Dixit
Publikováno v:
Nature. 587(7833)
Mutations in the death receptor FAS
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::32a6433d04a9fdc12527bc4bd484234e
https://pubmed.ncbi.nlm.nih.gov/33106621
https://pubmed.ncbi.nlm.nih.gov/33106621
Autor:
Jonathan N. Pruneda, Jane L. Wagstaff, Christina Gladkova, David Komander, Alexander F. Schubert, Stefan M.V. Freund
Publikováno v:
The EMBO Journal
The Ser/Thr protein kinase PINK1 phosphorylates the well‐folded, globular protein ubiquitin (Ub) at a relatively protected site, Ser65. We previously showed that Ser65 phosphorylation results in a conformational change in which Ub adopts a dynamic
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::59f6202a16e0087f1ada04e285774963
https://doi.org/10.1101/189027
https://doi.org/10.1101/189027
Publikováno v:
Nature
Summary The E3 ubiquitin ligase PARKIN (encoded by PARK2) and the protein kinase PINK1 (encoded by PARK6) are mutated in autosomal recessive juvenile Parkinsonism (AR-JP) and work together in the disposal of damaged mitochondria by mitophagy1–3. PI
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2de5f13dea31b1e5ff78168d3a3a7714
https://pubmed.ncbi.nlm.nih.gov/26416742
https://pubmed.ncbi.nlm.nih.gov/26416742
Publikováno v:
Nature. 526:728-728
Nature 524, 370–374 (2015); doi:10.1038/nature14879 The print and PDF versions of this Letter are correct, but the wrong HTML versions of Figs 1–4 and ED Figs 1–10 were used initially, owing to an in-house error; these have been corrected.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::46023ed7d20924e952152bc19077166f
https://doi.org/10.1038/nature15531
https://doi.org/10.1038/nature15531
Autor:
Jan Steyaert, Els Pardon, Sarah L. Maslen, Alexander F. Schubert, Stefan M.V. Freund, Christina Gladkova, Jane L. Wagstaff, David Komander
Publikováno v:
Nature
Autosomal-recessive juvenile Parkinsonism (AR-JP) is caused by mutations in a number of PARK genes, in particular the genes encoding the E3 ubiquitin ligase Parkin (PARK2, also known as PRKN) and its upstream protein kinase PINK1 (also known as PARK6
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::78dddeeb3c800be6eda47974666172cd